메뉴 건너뛰기




Volumn 585, Issue 2, 2011, Pages 381-384

Polyglutamine shows a urea-like affinity for unfolded cytosolic protein

Author keywords

Denaturation; Huntington's disease; Polyglutamine; Protein folding; Proteostasis; Urea

Indexed keywords

CYTOPLASM PROTEIN; POLYGLUTAMINE; UREA;

EID: 78651350812     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.12.023     Document Type: Article
Times cited : (14)

References (22)
  • 1
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: Protein misfolding revisited
    • A.J. Williams, and H.L. Paulson Polyglutamine neurodegeneration: protein misfolding revisited Trends Neurosci. 31 2008 521
    • (2008) Trends Neurosci. , vol.31 , pp. 521
    • Williams, A.J.1    Paulson, H.L.2
  • 2
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • DOI 10.1126/science.1124514
    • T. Gidalevitz, A. Ben-Zvi, K.H. Ho, H.R. Brignull, and R.I. Morimoto Progressive disruption of cellular protein folding in models of polyglutamine diseases Science 311 2006 1471 (Pubitemid 43376703)
    • (2006) Science , vol.311 , Issue.5766 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 3
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • DOI 10.1038/nature02998
    • M. Arrasate, S. Mitra, E.S. Schweitzer, M.R. Segal, and S. Finkbeiner Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death Nature 431 2004 805 (Pubitemid 39434070)
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 4
    • 55449095000 scopus 로고    scopus 로고
    • Molecular origin of polyglutamine aggregation in neurodegenerative diseases
    • S.D. Khare, F. Ding, K.N. Gwanmesia, and N.V. Dokholyan Molecular origin of polyglutamine aggregation in neurodegenerative diseases PLoS Comput. Biol. 1 2005 230
    • (2005) PLoS Comput. Biol. , vol.1 , pp. 230
    • Khare, S.D.1    Ding, F.2    Gwanmesia, K.N.3    Dokholyan, N.V.4
  • 5
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • R.J. Ellis Macromolecular crowding: obvious but underappreciated Trends Biochem. Sci. 26 2001 597
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597
    • Ellis, R.J.1
  • 8
    • 0029061516 scopus 로고
    • Protein stability as a function of denaturant concentration: The thermal stability of barnase in the presence of urea
    • C.M. Johnson, and A.R. Fersht Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea Biochemistry 34 1995 6795
    • (1995) Biochemistry , vol.34 , pp. 6795
    • Johnson, C.M.1    Fersht, A.R.2
  • 9
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • D. Kaganovich, R. Kopito, and J. Frydman Misfolded proteins partition between two distinct quality control compartments Nature 454 2008 1088
    • (2008) Nature , vol.454 , pp. 1088
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 10
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • A.L. Goldberg Protein degradation and protection against misfolded or damaged proteins Nature 426 2003 895
    • (2003) Nature , vol.426 , pp. 895
    • Goldberg, A.L.1
  • 11
    • 33645214602 scopus 로고    scopus 로고
    • Huntingtin and mutant SOD1 form aggregate structures with distinct molecular properties in human cells
    • DOI 10.1074/jbc.M509201200
    • G. Matsumoto, S. Kim, and R. Morimoto Huntingtin and mutant SOD1 for aggregate structures with distinct molecular properties in human cells J. Biol. Chem. 281 2006 4477 (Pubitemid 43847879)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 4477-4485
    • Matsumoto, G.1    Kim, S.2    Morimoto, R.I.3
  • 12
    • 35748947791 scopus 로고    scopus 로고
    • Regulation of stress-induced intracellular sorting and chaperone function of Hsp27 (HspB1) in mammalian cells
    • A.L. Bryantsev Regulation of stress-induced intracellular sorting and chaperone function of Hsp27 (HspB1) in mammalian cells Biochem. J. 407 2007 407
    • (2007) Biochem. J. , vol.407 , pp. 407
    • Bryantsev, A.L.1
  • 13
    • 20444413061 scopus 로고    scopus 로고
    • Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways
    • DOI 10.1016/j.cell.2005.03.024, PII S0092867405002965
    • A.J. McClellan, M.D. Scott, and J. Frydman Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways Cell 121 2005 739 (Pubitemid 40797596)
    • (2005) Cell , vol.121 , Issue.5 , pp. 739-748
    • McClellan, A.J.1    Scott, M.D.2    Frydman, J.3
  • 16
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils
    • A.E. Bevivino, and P.J. Loll An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates formation of parallel beta-fibrils Proc. Natl. Acad. Sci. USA 98 2001 11955
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11955
    • Bevivino, A.E.1    Loll, P.J.2
  • 17
    • 33744952750 scopus 로고    scopus 로고
    • Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent β barrel protein
    • DOI 10.1074/jbc.M511523200
    • Z. Ignatova, and L.M. Gierasch Extended polyglutamine tracts cause aggregation and structural perturbation of an adjacent beta barrel protein J. Biol. Chem. 281 2006 12959 (Pubitemid 43855389)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.18 , pp. 12959-12967
    • Ignatova, Z.1    Gierasch, L.M.2
  • 19
    • 24044492592 scopus 로고    scopus 로고
    • Effect of pH on thermal- and chemical-induced denaturation of GFP
    • DOI 10.1385/ABAB:126:2:149
    • K.M. Alkaabi, A. Yafea, and S.S. Ashraf Effect of pH on thermal- and chemical-induced denaturation of GFP Appl. Biochem. Biotech. 126 2005 149 (Pubitemid 41213294)
    • (2005) Applied Biochemistry and Biotechnology , vol.126 , Issue.2 , pp. 149-156
    • Alkaabi, K.M.1    Yafea, A.2    Ashraf, S.S.3
  • 20
    • 34250723399 scopus 로고    scopus 로고
    • Aqueous urea solutions: Structure, energetics, and urea aggregation
    • DOI 10.1021/jp066474n
    • M.C. Stumpe, and H. Grubmüller Aqueous urea solutions: structure, energetics, and urea aggregation J. Phys. Chem. B 111 2007 6220 (Pubitemid 46966229)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.22 , pp. 6220-6228
    • Stumpe, M.C.1    Grubmuller, H.2
  • 21
    • 0025169713 scopus 로고
    • Counteracting effects of urea and betaine in mammalian cells in culture
    • P.H. Yancey, and M.B. Burg Counteracting effects of urea and betaine in mammalian cells in culture Am. J. Physiol. 258 1990 R198
    • (1990) Am. J. Physiol. , vol.258 , pp. 198
    • Yancey, P.H.1    Burg, M.B.2
  • 22
    • 0036073289 scopus 로고    scopus 로고
    • Chemical chaperones reduce aggregate formation and cell death caused by the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch
    • DOI 10.1006/nbdi.2002.0502
    • H. Yoshida, T. Yoshizawa, F. Shibasaki, S. Shoji, and I. Kanazawa Chemical chaperones reduce aggregate formation and cell death caused by the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch Neurobiol. Dis. 10 2002 88 (Pubitemid 34775462)
    • (2002) Neurobiology of Disease , vol.10 , Issue.2 , pp. 88-99
    • Yoshida, H.1    Yoshizawa, T.2    Shibasaki, F.3    Shoji, S.4    Kanazawa, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.